Iron in PDB 3zqy: Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution- Non-Restraint Refinement

The structure of Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution- Non-Restraint Refinement, PDB code: 3zqy was solved by S.V.Antonyuk, N.Rustage, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.03
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	53.136, 53.136, 181.267, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution- Non-Restraint Refinement (pdb code 3zqy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution- Non-Restraint Refinement, PDB code: 3zqy:

Iron binding site 1 out of 1 in the Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution- Non-Restraint Refinement


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Prime From Alcaligenes Xylosoxidans: Carbon Monooxide Bound L16A Variant at 1.03 A Resolution- Non-Restraint Refinement within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe128 b:7.0 occ:1.00 FE A:HEC128 0.0 7.0 1.0 C A:CMO155 1.8 7.7 1.0 NE2 A:HIS120 2.0 8.0 1.0 ND A:HEC128 2.0 7.4 1.0 NB A:HEC128 2.0 7.0 1.0 NA A:HEC128 2.0 7.1 1.0 NC A:HEC128 2.0 6.9 1.0 O A:CMO155 2.8 12.3 1.0 C1B A:HEC128 3.0 7.6 1.0 CE1 A:HIS120 3.0 8.6 1.0 C4B A:HEC128 3.0 7.1 1.0 C1C A:HEC128 3.0 6.6 1.0 C4A A:HEC128 3.1 7.4 1.0 C4C A:HEC128 3.1 6.9 1.0 C1A A:HEC128 3.1 7.3 1.0 C1D A:HEC128 3.1 7.7 1.0 C4D A:HEC128 3.1 7.1 1.0 CD2 A:HIS120 3.1 8.4 1.0 HE1 A:HIS120 3.2 10.4 1.0 HD2 A:HIS120 3.3 10.1 1.0 CHB A:HEC128 3.4 8.2 1.0 CHD A:HEC128 3.4 7.0 1.0 CHC A:HEC128 3.4 7.3 1.0 CHA A:HEC128 3.4 7.9 1.0 HB2 A:ALA16 3.9 12.5 1.0 HH11 A:ARG124 4.1 14.3 1.0 ND1 A:HIS120 4.2 9.1 1.0 HE2 A:MET19 4.2 13.5 0.5 CG A:HIS120 4.2 8.9 1.0 HB3 A:ALA16 4.2 12.5 1.0 C3C A:HEC128 4.3 7.1 1.0 C3A A:HEC128 4.3 8.0 1.0 C2D A:HEC128 4.3 7.5 1.0 C2B A:HEC128 4.3 7.8 1.0 C2A A:HEC128 4.3 8.3 1.0 C3B A:HEC128 4.3 7.7 1.0 C3D A:HEC128 4.3 7.6 1.0 HH2 A:TRP56 4.3 11.4 1.0 C2C A:HEC128 4.3 7.1 1.0 HE1 A:MET19 4.4 13.5 0.5 HD3 A:ARG124 4.5 13.3 1.0 CB A:ALA16 4.6 8.3 1.0 NH1 A:ARG124 4.6 11.9 1.0 CE A:MET19 4.7 9.0 0.5 HE3 A:MET19 4.7 13.5 0.5 HH12 A:ARG124 4.8 14.3 1.0 HE2 A:MET19 4.9 17.1 0.5 HE3 A:MET19 4.9 17.1 0.5 HD1 A:HIS120 5.0 11.0 1.0 HB3 A:CYS116 5.0 11.4 1.0

S.V.Antonyuk, N.Rustage, C.A.Petersen, J.L.Arnst, D.J.Heyes, R.Sharma, N.G.Berry, N.S.Scrutton, R.R.Eady, C.R.Andrew, S.S.Hasnain. Carbon Monoxide Poisoning Is Prevented By the Energy Costs of Conformational Changes in Gas- Binding Haemproteins. Proc.Natl.Acad.Sci.Usa V. 108 15780 2011.
ISSN: ISSN 0027-8424
PubMed: 21900609
DOI: 10.1073/PNAS.1109051108